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In molecular biology, alpha-amylase inhibitor (or α-...) is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. This family of inhibitors has no action on plant and microbial alpha amylases. They are found in raw plants/herbs such as cinnamon and bacteria ...
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]
Phadebas is a synthetic biochemical substrate used for both qualitative and quantitative assessment of the α-amylase enzyme. Its active component is DSM-P, microspheres in which a blue dye has been chemically bound.
In the kinetic interaction of microparticle in solution (KIMS) and particle enhanced turbidimetric inhibition immunoassay (PETINIA), free antibodies bind to drug microparticle conjugates to form aggregates that absorb in the visible range in the absence of the analyte. In the presence of the analyte, the Ab binds to the free analyte, preventing ...
3,5-Dinitrosalicylic acid (DNS or DNSA, IUPAC name 2-hydroxy-3,5-dinitrobenzoic acid) is an aromatic compound that reacts with reducing sugars and other reducing molecules to form 3-amino-5-nitrosalicylic acid, which strongly absorbs light at 540 nm.
Alpha amylase, on the other hand, spikes quickly when confronted with a stressor and returns to baseline soon after the stress has passed, making salivary amylase measurement a powerful tool for psychological research studying acute stress responses. [12]
Coupled assay for hexokinase using glucose-6-phosphate dehydrogenase. Even when the enzyme reaction does not result in a change in the absorbance of light, it can still be possible to use a spectrophotometric assay for the enzyme by using a coupled assay. Here, the product of one reaction is used as the substrate of another, easily detectable ...
A common protocol used in the past for zymography of α-amylase activity was the so-called starch film protocol of W.W. Doane. Here a native PAGE gel was run to separate the proteins in a homogenate. Subsequently, a thin gel with starch dissolved (or more properly, suspended) in it was overlaid for a period of time on top of the original gel. [6]